DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-3, 6, 7, and 21-23 are pending in the application.
Applicant’s amendment to the claims, filed October 8, 2025, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s remarks filed October 8, 2025 in response to the non-final rejection mailed July 11, 2025 have been fully considered.
The text of those sections of Title 35 U.S. Code not included in the instant action can be found in a prior Office action.
Election/Restrictions
All pending claims are drawn to the elected invention of Group I. Claims 1-3, 6, 7, and 21-23 are being examined on the merits with claims 2, 6, and 7 being examined to the extent the claims read on the elected subject matter.
Claim Objections
Claim 1 is objected to for reciting the conjunction “and” between parts (e) and (f) and in the interest of improving claim form, it is suggested that the conjunction “and” between parts (e) and (f) be deleted and added between parts (f) and (g).
Claim Rejections - 35 USC § 112(b)
The rejection of claims 1-3, 6, 7, and 21-23 under 35 U.S.C. 112(b) as being indefinite for reciting “(e) a nucleic acid molecule encoding one or more enzymes capable of overproduction of L-phenylalanine to cinnamic acid by a phenylalanine ammonia lyase,” “(f) a nucleic acid molecule encoding one or more enzymes capable of converting cinnamic acid to coumaric acid by a cinnamate-4-hydroxylase,” and “ARO10 (phenylpyruvate decarboxylase)” and “PDC5 (pyruvate decarboxylase)” is withdrawn in view of the instant amendment to claim 1.
Claims 1-3, 6, 7, and 21-23 are newly rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention. This rejection is necessitated by the instant amendment to claim 1.
Claim 1 (claims 2, 3, 6, 7, and 21-23 dependent therefrom) is indefinite in the recitation of “said cinnamate-4-hydroxylase is functionally expressed with a compatible cytochrome P450 reductase” in part (f) because it is unclear as to the intended meaning of “functionally expressed with a compatible cytochrome P450 reductase.” The examiner has reviewed the specification for a definition or description of the intended meaning of the phrase “functionally expressed with a compatible cytochrome P450 reductase” in the context of part (f) of claim 1, however, there is no such definition or description. As written, the noted phrase has widely divergent interpretations including, e.g., the cinnamate-4-hydroxylase is expressed as a fusion protein with “a compatible cytochrome P450 reductase,” or that expression of the cinnamate-4-hydroxylase is under expression control of “a compatible cytochrome P450 reductase.” It is suggested that applicant clarify the meaning of the noted phrase.
Claim 21 is confusing in the recitation of “further comprising a nucleic acid molecule encoding a coumaroyl CoA ligase” because, as amended, claim 1 recites the narrower limitation of “a nucleic acid molecule encoding a coumaroyl CoA ligase that selectively ligates CoA to one or more of cinnamate, p-coumaric acid, caffeic acid, ferulic acid, or sinapic acid.” It is suggested that applicant clarify the inconsistency of claim 21 with the amended claim 1.
Claim Rejections - 35 USC § 112(a)
Claims 1-3, 6, 7, and 21-23 are newly rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, at the time the application was filed, had possession of the claimed invention. This is a new matter rejection and is necessitated by the instant amendment to claim 1.
MPEP § 2163.II.A.3.(b) states, “when filing an amendment an applicant should show support in the original disclosure for new or amended claims”. See also MPEP 714.02. MPEP § 2163.II.A.3.(b) further states, “[i]f the originally filed disclosure does not provide support for each claim limitation, or if an element which applicant describes as essential or critical is not claimed, a new or amended claim must be rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112, para. 1, as lacking adequate written description”. According to MPEP § 2163.I.B, “While there is no in haec verba requirement, newly added claim limitations must be supported in the specification through express, implicit, or inherent disclosure” and “The fundamental factual inquiry is whether the specification conveys with reasonable clarity to those skilled in the art that, as of the filing date sought, applicant was in possession of the invention as now claimed. See, e.g., Vas-Cath, Inc., 935 F.2d at 1563-64, 19 USPQ2d at 1117.”
As amended claim 1 (claims 2, 3, 6, 7, and 21-23 dependent therefrom) recites (in relevant part) “(c) a nucleic acid molecule encoding a tyrosine decarboxylase that selectively decarboxylates tyrosine over phenylalanine,” “(f) a nucleic acid molecule encoding a cinnamate-4-hydroxylase…wherein said cinnamate-4-hydroxylase is functionally expressed with a compatible cytochrome P450 reductase,” and “(g) a nucleic acid molecule encoding a coumaroyl CoA ligase that selectively ligates CoA to one or more of cinnamate, p-coumaric acid, caffeic acid, ferulic acid, or sinapic acid.”
According to the instant remarks at p. 6, “[s]upport for the claim amendments can be found in the specification as filed, for example at paragraphs n paragraphs [0041], [0046], [0047], [0057], and [0107].” However, there is no apparent descriptive support in the original application for the noted claim 1 limitations. Applicant is invited to show support for the limitations at issue.
Claim Rejections - 35 USC § 103
The rejection of claims 1, 2, 6, 7, and 21-23 under 35 U.S.C. 103 as being unpatentable over Hagel, J. (“Metabolic Engineering of Hydroxycinnamic Acid Amide in Nicotiana tabacum”, Dissertation, University of Calgary, 2004; cited on Form PTO-892 mailed on June 12, 2024; hereafter “Hagel”) in view of Kang et al. (Biotechnol. Lett. 31:1469-1475, 2009; cited on the IDS filed on November 2, 2022; hereafter “Kang”), Jiang, H. (“Metabolic Engineering of the Phenylpropanoid Pathway in Saccharomyces cerevisiae”, Dissertation, Purdue University, 2005; cited on Form PTO-892 mailed on June 12, 2024; hereafter “Jiang”), and Koopman et al. (Microbial Cell Factories 11:155, 2012, 15 pages; cited on the IDS filed on November 2, 2022; hereafter “Koopman”), and as evidenced by IUBMB Enzyme Nomenclature for EC 6.2.1.12 (obtained from https://iubmb.qmul.ac.uk/enzyme/EC6/2/1/12.html on January 30, 2025, 1 page; cited on Form PTO-892 mailed on February 4, 2025; hereafter “IUBMB”) and
the rejection of claim 3 under 35 U.S.C. 103 as being unpatentable over Hagel in view of Kang, Jiang, and Koopman and as evidenced by IUBMB as applied to claims 1, 2, 6, 7, and 21-23 above, and further in view of Katz et al. (US 2015/0361455 A1; cited on the IDS filed on November 2, 2022; hereafter “Katz”)
are withdrawn in view of the instant amendment to claim 1 to recite “wherein said cinnate-4-hydroxylase is functionally expressed with a compatible cytochrome P450 reductase.” The combination of Hagel, Kang, Jiang, Koopman, and Katz does not teach or suggest “cinnate-4-hydroxylase is functionally expressed with a compatible cytochrome P450 reductase.”
Claims 1, 2, 6, 7, and 21-23 are newly rejected under 35 U.S.C. 103 as being unpatentable over Hagel in view of Kang, Jiang, Trantas et al. (Metabolic Engineer. 11:355-366, 2009; cited on the attached Form PTO-892; hereafter “Trantas”) and Koopman, and as evidenced by IUBMB. This rejection is necessitated by the instant amendment to claim 1.
As amended, the claims are drawn to a recombinant eukaryotic host cell capable of producing a tyramine containing hydroxycinnamic acid amide, the recombinant eukaryotic host cell comprising:
one or more nucleic acid molecules encoding one or more enzymes capable of overproduction of L-tyrosine or L-phenylalanine, wherein at least one of said enzymes is a feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase;
one or more nucleic acid molecules encoding one or more enzymes of a phenylpropanoid CoA pathway for making a hydroxycinnamoyl-CoA ester;
a nucleic acid molecule encoding a tyrosine decarboxylase that selectively decarboxylates tyrosine over phenylalanine;
a nucleic acid molecule encoding a tyramine N-hydroxycinnamoyltransferase;
a nucleic acid molecule encoding a phenylalanine ammonia lyase to convert L-phenylalanine to cinnamic acid;
a nucleic acid molecule encoding a cinnamate-4-hydroxylase to convert cinnamic acid to coumaric acid, wherein said cinnamate-4-hydroxylase is functionally expressed with a compatible cytochrome P450 reductase;
a nucleic acid molecule encoding a coumaroyl CoA ligase that selectively ligates CoA to one or more of cinnamate, p-coumaric acid, caffeic acid, ferulic acid, or sinapic acid;
wherein the recombinant eukaryotic host cell is a recombinant yeast strain, and
wherein the recombinant eukaryotic host cell comprises a knockout of ARO10 and a knockout of PDC5.
The following explanation is provided for clarity of the record. The rejection refers to the enzyme abbreviations DAHP synthase, PAL, C4H, CPR, 4CL, TYDC, and THT.
DAHP synthase is the abbreviation for 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase and corresponds to “one or more enzymes capable of overproduction of L-tyrosine” in part (a) of claim 1.
TYDC is the abbreviation for tyrosine decarboxylase and corresponds to part (c) of claim 1.
THT is the abbreviation for tyramine N-hydroxycinnamoyltransferase and corresponds to part (d) of claim 1.
PAL is the abbreviation for phenylalanine ammonia lyase and corresponds to “one or more enzymes of a phenylpropanoid CoA pathway for making a hydroxycinnamoyl-CoA ester” in part (b) of claim 1 and “one or more enzymes capable of overproduction of L-phenylalanine to cinnamic acid by a phenylalanine ammonia lyase” in part (e) of claim 1.
C4H is the abbreviation for cinnamate-4-hydrolyase and corresponds to “one or more enzymes of a phenylpropanoid CoA pathway for making a hydroxycinnamoyl-CoA ester” in part (b) of claim 1 and “one or more enzymes capable of converting cinnamic acid to coumaric acid by a cinnamate-4-hydroxylase” in part (f) of claim 1.
CPR is the abbreviation for cytochrome P450 reductase and corresponds to “one or more enzymes of a phenylpropanoid CoA pathway for making a hydroxycinnamoyl-CoA ester” in part (b) of claim 1 and “a compatible cytochrome P450 reductase” in part (f) of claim 1.
4CL is the abbreviation for 4-coumarate:CoA ligase or as evidenced by IUBMB, is alternatively referred to as p-coumaroyl CoA ligase (see “Accepted name” and “Other name(s)”). 4CL corresponds to “one or more enzymes of a phenylpropanoid CoA pathway for making a hydroxycinnamoyl-CoA ester” in part (b) of claim 1 and “a coumaroyl CoA ligase that selectively ligates CoA to one or more of cinnamate, p-coumaric acid, caffeic acid, ferulic acid, or sinapic acid” in part (g) of claim 1.
TYDC is the abbreviation for tyrosine decarboxylase and corresponds to part (c) of claim 1.
THT is the abbreviation for tyramine N-hydroxycinnamoyltransferase and corresponds to part (d) of claim 1.
Figure 3 of Hagel shows a simplified scheme for the biosynthesis of the hydroxycinnamic acid amides, 4-coumaroyltyramine and feruloyltyramine, in plants (pp. 10-11). Hagel teaches important enzymes in the biosynthesis of hydroxycinnamic acid amides in plants including PAL, 4CL, TYDC, and THT (p. 14, bottom to p. 24, middle). Hagel teaches 4CL catalyzes the last step of the general phenylpropanoid pathway and converts 4-coumaric acid to the corresponding CoA ester (p. 15, first full paragraph). Figure 7 of Hagel show the phenylpropanoid pathway showing biosynthesis of hydroxycinnamic acid amides, which includes C4H to convert cinnamate to 4-coumarate (pp. 31-32). Hagel teaches a transgenic tobacco plant designated as “TYDC x THT,” which is engineered to overexpress TYDC and THT for the increased production of tyramine-derived hydroxycinnamic acid amide (p. iii, Abstract; p. 49, second paragraph).
Hagel teaches engineering a tobacco plant for production of tyramine-derived hydroxycinnamic acid amide but does not teach a recombinant yeast strain for production of hydroxycinnamic acid amides.
Kang teaches that tyramine derivatives are synthesized in trace amounts in plants and that in contrast to using plants as hosts for producing plant specific secondary metabolites, the use of microbes provides a good alternative for the mass production of scarce bioactive compounds (p. 1469, column 1, bottom to p. 1470, column 2, top). Kang teaches an E. coli modified to express 4CL and THT, which, when combined with tyramine, produced large amounts of feruloyltyramine, 4-coumaroyltyramine, and caffeoyltyramine (p. 1470, sentence bridging columns 1-2).
Jiang teaches that S. cerevisiae has some advantages over E. coli for expressing eukaryotic heterologous proteins (p. 14, bottom). Jiang teaches the phenylpropanoid pathway in plants (p. 10, Figure 1.2) including PAL, C4H, and 4CL (p. 16, middle). Jiang suggests transferring a plant phenylpropanoid pathway into yeast for the production of desired downstream products (p. 16, middle).
Trantas teaches S. cerevisiae as a eukaryotic organism has transcriptional and translational mechanisms similar in basic respects to those of plants and this would make yeast a suitable single-celled organism for the production of secondary metabolites through the heterologous expression of plant genes (p. 361, column 2, bottom). Similar to Jiang, Trantas discusses the phenylpropanoid pathway in plants including PAL, C4H, and 4CL (p. 356, column 1, middle). Trantas teaches a metabolically engineered S. cerevisiae strain expressing PAL, C4H, 4CL, and CPR for production of downstream products from the intermediate 4-coumaroyl-CoA (p. 360, Figure 2), noting the productivity of the C4H required co-expression with CPR for maximal production of p-coumaric acid (p. 359, column 2, middle; p. 360, Figure 2).
In view of the combined teachings of Hagel, Kang, Jiang, and Trantas, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the S. cerevisiae expressing phenylpropanoid pathway enzymes PAL, C4H, and 4CL of Trantas by co-expressing TYDC and THT in order to produce hydroxycinnamic acid amides.
One would have been motivated to do so because while Hagel teaches recombinantly expressing TYDC and THT in a plant in order to convert 4-coumaroyl-CoA of the phenylpropanoid pathway and tyramine to hydroxycinnamic acid amides, Kang teaches that tyramine derivatives are synthesized in only trace amounts in plants. As an alternative, Kang teaches using microbes for the mass production of scarce bioactive compounds, and while Kang selected E. coli as the microbe for production of hydroxycinnamic acid amides, Jiang acknowledges that S. cerevisiae has advantages over E. coli for expression of eukaryotic genes and Trantas teaches S. cerevisiae as a eukaryotic organism has transcriptional and translational mechanisms similar in basic respects to those of plants and this would make yeast a suitable single-celled organism for the production of secondary metabolites through the heterologous expression of plant genes. Trantas teaches a metabolically engineered S. cerevisiae comprising the plant phenylpropanoid pathway PAL, C4H, 4CL, and CPR to produce the 4-coumaroyl-CoA intermediate as a metabolite for biosynthesis of plant-based compounds.
One would have expected success because the TYDC and THT taught by Hagel and Kang are eukaryotic enzymes and Jiang taught S. cerevisiae as a suitable host for the expression of eukaryotic polypeptides and Trantas taught S. cerevisiae as a eukaryotic organism has transcriptional and translational mechanisms similar in basic respects to those of plants and this would make yeast a suitable single-celled organism for the production of secondary metabolites through the heterologous expression of plant genes.
Regarding the limitation “a tyrosine decarboxylase that selectively decarboxylates tyrosine over phenylalanine” in part (c) of claim 1, by virtue of its name as a “tyrosine decarboxylase,” one of ordinary skill in the art would have recognized that TYDC preferentially decarboxylates tyrosine over phenylalanine. Moreover, Hagel teaches TYDC catalyzes the irreversible decarboxylation of tyrosine (p. 15, bottom) with an exclusive substrate specificity for phenol side chain (p. 16, top). As such, one of ordinary skill in the art would have recognized that TYDC selectively decarboxylates tyrosine over phenylalanine.
Regarding the limitation “a coumaroyl CoA ligase that selectively ligates CoA to one or more of cinnamate, p-coumaric acid, caffeic acid, ferulic acid, or sinapic acid,” Trantas teaches various plant 4CL enzymes expressed in S. cerevisiae to catalyze the conversion of p-coumaric acid to its corresponding CoA product (p. 362, Table 3) and Jiang teaches At4CL1, which is a 4CL from Arabidopsis thaliana and catalyzes the conversion of p-coumaric acid, ferulic acid, and caffeic acid to their corresponding CoA products (p. 83, second paragraph).
Regarding the limitations “(a) one or more nucleic acid molecules encoding one or more enzymes capable of overproduction of L-tyrosine or L-phenylalanine, wherein at least one of said enzymes is a feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase” and “wherein the recombinant eukaryotic host cell comprises a knockout of ARO10 and a knockout of PDC5,” as shown by Hagel, tyrosine and phenylalanine are substrates for hydroxycinnamic acid amide production (p. 10 and Figure 3) and Jiang teaches that L-Tyr pool size is limiting in S. cerevisiae overexpressing PAL (p. 59) and the S. cerevisiae could be engineered to increase flux to L-Phe and L-Tyr (p. 98, bottom). Jiang teaches a DAHP synthase mutant free from feedback inhibition and expressing the mutant DAHP synthase increased L-Tyr production (p. 99). Koopman teaches expressing a mutant DAHP synthase in S. cerevisiae and knocking out ARO10 and PDC5 to enhance the availability of the aromatic amino acids L-Phe and L-Tyr (p. 5, columns 1-2).
In view of the teachings of Jiang and Koopman, it would have been obvious to one of ordinary skill in the art before the effective filing date to further modify the S. cerevisiae of Trantas to express a feedback-resistant DAHP synthase and to knockout ARO10 and PDC5.
One would have been motivated and would have expected success to do so because Hagel taught tyrosine phenylalanine are substrates for hydroxycinnamic acid amide production, Jiang taught the S. cerevisiae could be engineered to increase flux to L-Phe and L-Tyr, which are aromatic amino acids, Jiang and Koopman taught expressing a feedback-resistant DAHP synthase to increase aromatic amino acid production, and Koopman taught knocking out ARO10 and PDC5 to reduce the diversion of aromatic amino acid biosynthesis.
Regarding claim 21, the S. cerevisiae expressing enzymes of a phenylpropanoid pathway of Trantas modified to co-express TYDC and THT comprises nucleic acids encoding 4CL, C4H, and CPR.
Therefore, claims 1, 2, 6, 7, and 21-23 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 3 is newly rejected under 35 U.S.C. 103 as being unpatentable over Hagel in view of Kang, Jiang, Trantas, and Koopman and as evidenced by IUBMB as applied to claims 1, 2, 6, 7, and 21-23 above, and further in view of Katz.
Claim 3 is drawn to the recombinant eukaryotic host cell of claim 1, wherein said host cell further overproduces methionine.
The relevant teachings of Hagel, Kang, Jiang, Trantas, and Koopman and evidentiary references IUBMB as applied to claims 1, 2, 6, 7, and 21-23 are set forth above.
The combination of Hagel, Kang, Jiang, Trantas, and Koopman does not teach or suggest overproducing methionine.
Similar to Jiang and Trantas, Katz teaches recombinant expression of enzymes of the plant phenylpropanoid pathway to supply the necessary CoA precursor for desired biosynthesis (paragraph [0003] and Figure 2). Katz teaches the plasmid for recombinant enzyme expression comprises a gene involved in methionine biosynthesis and teaches selecting transformants comprising the plasmid that are auxotrophic for methionine by culturing in a minimal medium lacking methionine (paragraphs [0129], [0134], and [0135]).
In view of the combined teachings of Hagel, Kang, Jiang, Trantas, Koopman, and Katz, it would have been obvious to one of ordinary skill in the art before the effective filing date to further modify the S. cerevisiae of Trantas to be auxotrophic for methionine and to co-express a gene involved in methionine biosynthesis. One would have been motivated to and would have had a reasonable expectation of success to do this because of the selection method taught by Katz for selecting transformants that recombinantly express enzymes of a plant phenylpropanoid pathway for biosynthesis of a desired plant compound.
Therefore, claim 3 would have been obvious to one of ordinary skill in the art before the effective filing date.
RESPONSE TO REMARKS: Beginning at p. 7 of the remarks, applicant argues the rejections are obviated by the amendment to claim 1 to recite features that are not taught or suggested by the cited prior art including the recitation of a feedback resistant DAHP. According to applicant, there would have been no motivation to express a feedback resistant DAHP.
Applicant’s argument is not found persuasive. Contrary to applicant’s position, the combination of references teaches and/or suggests expressing a feedback resistant DAHP. As stated above, Hagel shows tyrosine and phenylalanine are substrates for hydroxycinnamic acid amide production (p. 10 and Figure 3); Jiang teaches that L-Tyr pool size is limiting in S. cerevisiae expressing PAL (p. 59); Jiang teaches the S. cerevisiae could be engineered to increase flux to L-Phe and L-Tyr (p. 98, bottom); Jiang teaches a DAHP synthase mutant free from feedback inhibition and expressing the mutant DAHP synthase increased L-Tyr production (p. 99); and Koopman teaches expressing a mutant DAHP synthase in S. cerevisiae and knocking out ARO10 and PDC5 to enhance the availability of the aromatic amino acids L-Phe and L-Tyr (p. 5, columns 1-2). In view of these teachings, one of ordinary skill in the art would have been motivated to modify the S. cerevisiae of Trantas to express a feedback resistant DAHP.
At p. 8 of the remarks, applicant argues the cited combination of prior art would lead to a system that is unsatisfactory for its intended purpose because Kang teaches the THT acts on dopamine and tyramine, which leads to the production of dopamine-derived byproducts, while the claims employ highly selective enzymes to prevent formation of byproducts. According to applicant, combining the enzymes of the prior art would have resulted in the production of a mixture of products including undesirable byproducts.
Applicant’s argument is not found persuasive. Kang teaches studies of THT enzyme kinetics have shown that THT enzymes prefer tyramine as the optimal acyl acceptor substrate while displaying low affinities toward other amines such as dopamine (p. 1469, column 2, middle) and dopamine derivatives were only produced when exogenous dopamine was added as a substrate and even then, compared to tyramine derivatives dopamine derivatives were only synthesized at low levels (p. 1472, paragraph bridging columns 1-2). Given that the S. cerevisiae of Trantas modified to express TYDC for the production of tyramine and does not comprise an enzymatic pathway for dopamine production, one of ordinary skill in the art would have expected Trantas’ modified S. cerevisiae to produce tyramine derivatives and to produce no dopamine derivative byproducts.
Beginning at p. 8 of the remarks, applicant argues claim 1 is amended to recite functional expression of cinnamate-4-hydroxylase with a compatible cytochrome P450 reductase. Applicant argues Kang and Jiang teach away from functionally expressing cinnamate-4-hydroxylase with a compatible cytochrome P450 reductase.
Applicant’s argument is not found persuasive. As stated above, Trantas teaches a metabolically engineered S. cerevisiae strain expressing PAL, C4H, 4CL, and CPR (p. 360, Figure 2) and acknowledges that the productivity of the C4H required co-expression with CPR for maximal production of p-coumaric acid (p. 359, column 2, middle; p. 360, Figure 2).
For these reasons, it is the examiner’s position that the claimed invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date.
Conclusion
Status of the claims:
Claims 1-3, 6, 7, and 21-23 are pending in the application.
Claims 1-3, 6, 7, and 21-23 are rejected.
No claim is in condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656